细粒棘球绦虫蛋白egG1y162-1、egG1y162-2的抗原表位比较
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摘要
目的分析蛋白egG1y162-1、egG1y162-2的氨基酸序列,了解其理化性质及二级结构特点,预测比较其抗原表位,为包虫病的免疫学诊断及表位疫苗的研制提供理论依据。方法采用生物信息学技术,利用在线软件ProtParam分析egG1y162-1和egG1y162-2的理化性质,使用DNAstar软件的protean等程序分析egG1y162-1和egG1y162-2蛋白的二级结构特点,运用在线软件IEDB等对egG1y162-1和egG1y162-2蛋白各参数进行综合分析并预测其抗原表位。结果综合分析各参数预测egG1y162-1的优势B细胞表位为9～28位氨基酸残基(LTKELKTTLPEHFRWIHVGS),egG1y162-1上29～36位氨基酸残基(RSLELGWN)区域可能存在人鼠共同T细胞抗原表位;egG1y162-2的优势B细胞表位为25～39位氨基酸残基(EGLKPSTFYEVVVQAFKGGS)、41～60位氨基酸残基(KGGSQVFKYTGFIRTLAPGE),egG1y162-2上26～41位氨基酸残基(GLKPSTFYEVVVQAFK)区域可能存在人鼠共同T细胞抗原表位。结论通过对细粒棘球绦虫蛋白egG1y162-1、egG1y162-2进行抗原表位分析,发现二者均存在评分较高的优势T表位和B表位,且存在人鼠共同T表位,而egG1y162-2的各方面指标要优于egG1y162-1,这对包虫病的诊断和疫苗研究有重要意义。
Objective The amino acid sequences of egG1y162-1and egG1y162-2 were analyzed to learn about the physicochemical properties and secondary structure characteristics and predict the epitopes of egG1y162-1and egG1y162-2,which aimed to provided theoretical basis for the immunological diagnosis of echinococcosis and the development of epitope vaccines.Methods The physicochemical properties of egG1y162-1and egG1y162-2were analyzed by ProtParam Bioinformatics technology.The secondary structure characteristics of egG1y162-1and egG1y162-2were analyzed by DNAstar protean,and the parameters of the egG1y162-1and egG1y162-2analyzed by IEDB,and predicted its antigen epitopes.Results Based on a comprehensive analysis of the parameters,the dominant B cell epitope of egG1y162-1is 9-28 amino acid residues(LTKELKTTLPEHFRWIHVGS),and the amino acid residues 29-36(RSLELGWN)of egG1y162-1may exist commonly in human and mouse T cell epitopes.The dominant B cell epitope of egG1y162-2is 25-39 amino acid residues(EGLKPSTFYEVVVQAFKGGS),41-60 amino acid residues(KGGSQVFKYTGFIRTLAPGE),and 2-41 amino acid residues(GLKPSTFYEVVVQAFK).Conclusion By analyzing the epitopes of Echinococcus granulosus proteins egG1y162-1and egG1y162-2,the result showed there are dominant T and B epitopes with higher scores,and commonly in human and mouse T cell epitopes.All aspects of egG1y162-2are superior to egG1y162-1,which is important for the diagnosis of echinococcosis and research of vaccination.
Objective The amino acid sequences of egG1y162-1and egG1y162-2 were analyzed to learn about the physicochemical properties and secondary structure characteristics and predict the epitopes of egG1y162-1and egG1y162-2,which aimed to provided theoretical basis for the immunological diagnosis of echinococcosis and the development of epitope vaccines.Methods The physicochemical properties of egG1y162-1and egG1y162-2were analyzed by ProtParam Bioinformatics technology.The secondary structure characteristics of egG1y162-1and egG1y162-2were analyzed by DNAstar protean,and the parameters of the egG1y162-1and egG1y162-2analyzed by IEDB,and predicted its antigen epitopes.Results Based on a comprehensive analysis of the parameters,the dominant B cell epitope of egG1y162-1is 9-28 amino acid residues(LTKELKTTLPEHFRWIHVGS),and the amino acid residues 29-36(RSLELGWN)of egG1y162-1may exist commonly in human and mouse T cell epitopes.The dominant B cell epitope of egG1y162-2is 25-39 amino acid residues(EGLKPSTFYEVVVQAFKGGS),41-60 amino acid residues(KGGSQVFKYTGFIRTLAPGE),and 2-41 amino acid residues(GLKPSTFYEVVVQAFK).Conclusion By analyzing the epitopes of Echinococcus granulosus proteins egG1y162-1and egG1y162-2,the result showed there are dominant T and B epitopes with higher scores,and commonly in human and mouse T cell epitopes.All aspects of egG1y162-2are superior to egG1y162-1,which is important for the diagnosis of echinococcosis and research of vaccination.
引文
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[11]LI Y H,LIU X F,ZHU Y J,et al.Bioinformatic prediction of epitopes in the Emy162antigen of Echinococcus multilocularis[J].Exp Ther Med,2013,6(2):335-340.
[12]安梦婷,吾拉木·马木提,马海梅,等.细粒棘球蚴AgB1、AgB2、AgB4抗原表位的特性分析[J].新疆医科大学学报,2016,39(12):1541-1546,1553.
[2]潘卫庆,汤林华.分子寄生虫学[M].上海科学技术出版社,2004:345-399.
[3]曹春宝,马秀敏,丁剑冰,等.细粒棘球蚴egG1Y162抗原基因的克隆及蛋白质序列分析[J].中国病原生物学杂志,2008,3(12):903-906.
[4]祖力皮也·吐尔逊,曹春宝,温浩,等.细粒棘球蚴EgG1Y162基因进化分析、表达及鉴定[J].中国生物工程杂志,2016,36(4):78-87.
[5]ZHANG F B,MA X M,DING J B,et al.Identification,expression and phylogenetic analysis of EgG1Y162from Echinococcus granulosus.[J].Int J Clin Exp Patho,2014,7(9):5655-5664.
[6]ZHANG F B,LI S Y,DING J B,et al.Immunization of mice with egG1Y162-1/2provides protection against Echinococcus granulosus,infection in BALB/c mice[J].Mol Immunol,2018,94:183-189.
[7]马海梅,吾拉木·马木提,张峰波,等.新疆细粒棘球绦虫EgAgB8/3蛋白的生物信息学分析及意义[J].中国医药导报,2017,14(14):8-11.
[8]李玉娇,王晶,丁剑冰,等.细粒棘球绦虫Eg95抗原表位的生物信息学预测[J].中国人兽共患病学报,2011,27(10):892-896,900.
[9]李玉娇,杨晶,赵慧,等.细粒棘球绦虫EgA31重组蛋白的抗原表位分析预测[J].中国寄生虫学与寄生虫病杂志,2012,30(1):78-80.
[10]刘献飞,丁剑冰,李玉娇,等.多房棘球绦虫95抗原T-B联合表位分析[J].中国病原生物学杂志,2012,7(10):770-773,786.
[11]LI Y H,LIU X F,ZHU Y J,et al.Bioinformatic prediction of epitopes in the Emy162antigen of Echinococcus multilocularis[J].Exp Ther Med,2013,6(2):335-340.
[12]安梦婷,吾拉木·马木提,马海梅,等.细粒棘球蚴AgB1、AgB2、AgB4抗原表位的特性分析[J].新疆医科大学学报,2016,39(12):1541-1546,1553.